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1.A.23.2.1
Major MscS channel protein, YggB. Seven residues, mostly hydrophobic, in the first and second transmembrane helices are lipid-sensing residues (Malcolm et al., 2011).  X-ray structures are available (Lai et al. 2013).  The cytoplasmic cage domain senses macromolecular crowding (Rowe et al. 2014). A gating mechanism has been proposed (Malcolm et al. 2015).  The thermodynamics of K+ leak have been studied (Koprowski et al. 2015).  In the MscS crystal structure (PDB 2OAU ), a narrow, hydrophobic opening is visible in the crystal structure, and a vapor lock, created by hydrophobic seals consisting of L105 and L109, is the barrier to water and ions (Rasmussen et al. 2015). The voltage dependence of inactivation occurs independently of the positive charges of R46, R54, and R74 (Nomura et al. 2016).

Accession Number:P0C0S1
Protein Name:Small-conductance mechanosensitive channel YggB aka B2924
Length:286
Molecular Weight:30896.00
Species:Escherichia coli [83333]
Number of TMSs:4
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Multi-pass membrane protein2
Substrate ions

Cross database links:

Genevestigator: P0C0S1
EchoBASE: EB1149
EcoGene: EG11160
eggNOG: COG0668
HEGENOM: HBG691319
DIP: DIP-36192N
RefSeq: AP_003482.1    NP_417399.1   
Entrez Gene ID: 947416   
Pfam: PF00924    PF05552   
BioCyc: EcoCyc:EG11160-MONOMER    ECOL168927:B2924-MONOMER   
KEGG: ecj:JW2891    eco:b2924   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0008381 F:mechanically-gated ion channel activity
GO:0009992 P:cellular water homeostasis
GO:0006811 P:ion transport
GO:0055085 P:transmembrane transport

References (15)

[1] “Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli.”  Alefounder P.R.et.al.   2546007
[2] “The complete genome sequence of Escherichia coli K-12.”  Blattner F.R.et.al.   9278503
[3] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.”  Hayashi K.et.al.   16738553
[4] “Pressure-sensitive ion channel in Escherichia coli.”  Martinac B.et.al.   2436228
[5] “Characterization of mechanosensitive channels in Escherichia coli cytoplasmic membrane by whole-cell patch clamp recording.”  Cui C.et.al.   7595939
[6] “Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: identification of genes required for MscS activity.”  Levina N.et.al.   10202137
[7] “Purification of the small mechanosensitive channel of Escherichia coli (MscS): the subunit structure, conduction, and gating characteristics in liposomes.”  Sukharev S.et.al.   12080120
[8] “Functional design of bacterial mechanosensitive channels. Comparisons and contrasts illuminated by random mutagenesis.”  Okada K.et.al.   12015316
[9] “C termini of the Escherichia coli mechanosensitive ion channel (MscS) move apart upon the channel opening.”  Koprowski P.et.al.   12551944
[10] “The closed structure of the MscS mechanosensitive channel. Cross-linking of single cysteine mutants.”  Miller S.et.al.   12767977
[11] “The conserved carboxy-terminus of the MscS mechanosensitive channel is not essential but increases stability and activity.”  Schumann U.et.al.   15304354
[12] “Protein complexes of the Escherichia coli cell envelope.”  Stenberg F.et.al.   16079137
[13] “Global topology analysis of the Escherichia coli inner membrane proteome.”  Daley D.O.et.al.   15919996
[14] “Pivotal role of the glycine-rich TM3 helix in gating the MscS mechanosensitive channel.”  Edwards M.D.et.al.   15665866
[15] “Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel.”  Bass R.B.et.al.   12446901
Structure:
2OAU   2VV5   3UDC   4AGE   4AGF   4HWA   5AJI     

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FASTA formatted sequence
1:	MEDLNVVDSI NGAGSWLVAN QALLLSYAVN IVAALAIIIV GLIIARMISN AVNRLMISRK 
61:	IDATVADFLS ALVRYGIIAF TLIAALGRVG VQTASVIAVL GAAGLAVGLA LQGSLSNLAA 
121:	GVLLVMFRPF RAGEYVDLGG VAGTVLSVQI FSTTMRTADG KIIVIPNGKI IAGNIINFSR 
181:	EPVRRNEFII GVAYDSDIDQ VKQILTNIIQ SEDRILKDRE MTVRLNELGA SSINFVVRVW 
241:	SNSGDLQNVY WDVLERIKRE FDAAGISFPY PQMDVNFKRV KEDKAA